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Protein crystallization is the process of formation of a regular array of individual protein molecules stabilized by crystal contacts. If the crystal is sufficiently ordered, it will diffract . Some proteins naturally form crystalline arrays, like aquaporin in the lens of the eye.
Salting out (also known as salt-induced precipitation, salt fractionation, anti-solvent crystallization, precipitation crystallization, or drowning out) [1] is a purification technique that utilizes the reduced solubility of certain molecules in a solution of very high ionic strength.
Ammonium sulfate is an inorganic salt with a high solubility that disassociates into ammonium (NH + 4) and sulfate (SO 2− 4) in aqueous solutions. [1] Ammonium sulfate is especially useful as a precipitant because it is highly soluble, stabilizes protein structure, has a relatively low density, is readily available, and is relatively inexpensive.
Ammonium sulfate precipitation is a common method for protein purification by precipitation. As the ionic strength of a solution increases, the solubility of proteins in that solution decreases. Being extremely soluble in water, ammonium sulfate can "salt out" (precipitate) proteins from aqueous solutions.
Streak seeding [1] is a method first described during ICCBM-3 by Enrico Stura to induce crystallization in a straight line into a sitting or hanging drop for protein crystallization by introducing microseeds. The purpose is to control nucleation and understand the parameters that make crystals grow. It is also used to test any particular set of ...
Crystallization is the process by which solids form, where the atoms or molecules are highly organized into a structure known as a crystal.Some ways by which crystals form are precipitating from a solution, freezing, or more rarely deposition directly from a gas.
Water of crystallization can generally be removed by heating a sample but the crystalline properties are often lost. Compared to inorganic salts, proteins crystallize with large amounts of water in the crystal lattice. A water content of 50% is not uncommon for proteins.
For protein crystals this method is conducted by soaking the crystal of a sample to be analyzed with a heavy atom solution or co-crystallization with the heavy atom. The addition of the heavy atom (or ion) to the structure should not affect the crystal formation or unit cell dimensions in comparison to its native form, hence, they should be ...